117631 20240319081010.0 doi 10.1021/acs.jpcb.1c09911 sideral 129225 ART-2022-129225 eng Urriolabeitia, Asier Universidad de Zaragoza (orcid)0000-0001-9352-6922 Influence of the nonprotein amino acid mimosine in peptide conformational propensities from novel amber force field parameters 2022 Access copy available to the general public Unrestricted Mimosine is a nonprotein amino acid derived from plantsknown for its ability to bind to divalent and trivalent metal cations suchas Zn2+, Ni2+, Fe2+, orAl3+. This results in interesting antimicrobial andanticancer properties, which make mimosine a promising candidate fortherapeutic applications. One possibility is to incorporate mimosine intosynthetic short peptide drugs. However, how this amino acid affects thepeptide structure is not well understood, reducing our ability to designeffective therapeutic compounds. In this work, we used computersimulations to understand this question. Wefirst built parameters for themimosine residue to be used in combination with two classical forcefields of the Amber family. Then, we used atomistic molecular dynamicssimulations with the resulting parameter sets to evaluate the influence ofmimosine in the structural propensities for this amino acid. We comparedthe results of these simulations with homologous peptides, wheremimosine is replaced by either phenylalanine or tyrosine. We found that the strong dipole in mimosine induces a preference forconformations where the amino acid rings are stacked over more extended conformations. We validated our results using quantummechanical calculations, which provide a robust foundation for the outcome of our classical simulations info:eu-repo/grantAgreement/ES/MECD/FPU17-05417 info:eu-repo/grantAgreement/ES/MINECO/PGC2018-099321-B-I00 info:eu-repo/semantics/openAccess by http://creativecommons.org/licenses/by/3.0/es/ 3.3 2022 CHEMISTRY, PHYSICAL 88 / 161 = 0.547 2022 Q3 T2 0.795 2022 Materials Chemistry 2022 Q1 Surfaces, Coatings and Films 2022 Q1 Physical and Theoretical Chemistry 2022 Q1 Medicine (miscellaneous) 2022 Q2 5.6 2022 info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion De Sancho, David Lopez, Xabier 2012 755 Universidad de Zaragoza Dpto. Química Física Área Química Física 126, 16 (2022), 2959-2967 J. phys. chem., B Journal of physical chemistry. B 1520-6106 3196347 http://zaguan.unizar.es/record/117631/files/texto_completo.pdf Versión publicada 2746598 http://zaguan.unizar.es/record/117631/files/texto_completo.jpg?subformat=icon icon Versión publicada oai:zaguan.unizar.es:117631 articulos driver 2024-03-18-15:00:33 ARTICLE